Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn, 12618, Estonia.
J Pept Sci. 2013 Jun;19(6):386-91. doi: 10.1002/psc.2513. Epub 2013 Apr 23.
Many peptides and proteins can form fibrillar aggregates in vitro, but only a limited number of them are forming pathological amyloid structures in vivo. We studied the fibrillization of four peptides--Alzheimer's amyloid-β (Aβ) 1-40 and 1-42, amylin and insulin. In all cases, intensive mechanical agitation of the solution initiated fast fibrillization. However, when the mixing was stopped during the fibril growth phase, the fibrillization of amylin and insulin was practically stopped, and the rate for Aβ40 substantially decreased, whereas the fibrillization of Aβ42 peptide continued to proceed with almost the same rate as in the agitated conditions. The reason for the different sensitivity of the in vitro fibrillization of these peptides towards agitation in the fibril growth phase remains elusive.
许多肽和蛋白质在体外可以形成纤维状聚集物，但只有有限数量的肽和蛋白质在体内形成病理性的淀粉样结构。我们研究了四种肽——阿尔茨海默病淀粉样-β（Aβ）1-40 和 1-42、淀粉样蛋白和胰岛素的纤维化过程。在所有情况下，溶液的剧烈机械搅拌都会引发快速纤维化。然而，当在纤维生长阶段停止混合时，淀粉样蛋白和胰岛素的纤维化实际上停止了，Aβ40 的速度大大降低，而 Aβ42 肽的纤维化继续以与搅拌条件几乎相同的速度进行。这些肽在体外纤维化过程中对纤维生长阶段搅拌的不同敏感性的原因仍不清楚。
